(data stored in ACNUC9435 zone)

SWISSPROT: GLPK_RUEPO

ID   GLPK_RUEPO              Reviewed;         492 AA.
AC   Q5LWR1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   11-DEC-2019, entry version 91.
DE   RecName: Full=Glycerol kinase {ECO:0000255|HAMAP-Rule:MF_00186};
DE            EC=2.7.1.30 {ECO:0000255|HAMAP-Rule:MF_00186};
DE   AltName: Full=ATP:glycerol 3-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00186};
DE   AltName: Full=Glycerokinase {ECO:0000255|HAMAP-Rule:MF_00186};
DE            Short=GK {ECO:0000255|HAMAP-Rule:MF_00186};
GN   Name=glpK {ECO:0000255|HAMAP-Rule:MF_00186}; OrderedLocusNames=SPO0104;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- FUNCTION: Key enzyme in the regulation of glycerol uptake and
CC       metabolism. Catalyzes the phosphorylation of glycerol to yield sn-
CC       glycerol 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00186}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate;
CC         Xref=Rhea:RHEA:21644, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57597, ChEBI:CHEBI:456216;
CC         EC=2.7.1.30; Evidence={ECO:0000255|HAMAP-Rule:MF_00186};
CC   -!- ACTIVITY REGULATION: Inhibited by fructose 1,6-bisphosphate (FBP).
CC       {ECO:0000255|HAMAP-Rule:MF_00186}.
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00186}.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00186}.
DR   EMBL; CP000031; AAV93435.1; -; Genomic_DNA.
DR   RefSeq; WP_011045877.1; NC_003911.12.
DR   SMR; Q5LWR1; -.
DR   STRING; 246200.SPO0104; -.
DR   PRIDE; Q5LWR1; -.
DR   EnsemblBacteria; AAV93435; AAV93435; SPO0104.
DR   KEGG; sil:SPO0104; -.
DR   eggNOG; ENOG4108JQ0; Bacteria.
DR   eggNOG; COG0554; LUCA.
DR   HOGENOM; HOG000222134; -.
DR   KO; K00864; -.
DR   OMA; FMLMNIG; -.
DR   OrthoDB; 233605at2; -.
DR   BioCyc; RPOM246200:G1G48-105-MONOMER; -.
DR   UniPathway; UPA00618; UER00672.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004370; F:glycerol kinase activity; ISS:UniProtKB.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006071; P:glycerol metabolic process; ISS:UniProtKB.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00186; Glycerol_kin; 1.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018485; Carb_kinase_FGGY_C.
DR   InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR   InterPro; IPR018484; Carb_kinase_FGGY_N.
DR   InterPro; IPR005999; Glycerol_kin.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   PIRSF; PIRSF000538; GlpK; 1.
DR   TIGRFAMs; TIGR01311; glycerol_kin; 1.
DR   PROSITE; PS00445; FGGY_KINASES_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5LWR1.
DR   SWISS-2DPAGE; Q5LWR1.
KW   ATP-binding; Glycerol metabolism; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..492
FT                   /note="Glycerol kinase"
FT                   /id="PRO_1000020788"
FT   NP_BIND         11..13
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   NP_BIND         407..411
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   REGION          81..82
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   REGION          240..241
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         11
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         15
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         133
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         262
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         305
FT                   /note="ATP; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         309
FT                   /note="ATP; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT   BINDING         324
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
SQ   SEQUENCE   492 AA;  53036 MW;  6DAD0DE44B598658 CRC64;
     MTFILAIDQG TTSSRAILFD GEMRRVATAQ REFTQHFPEA GWVEHDAEEI WQTTVEVCRE
     VIAGQGIGPE QIAGIGITNQ RETTVVWDKA GGAPVHRAIV WQDRRTAAIC ERLRHAGCED
     DFTAQTGLLL DPYFSGTKVK WILDTVPGAR DRAAAGELLF GTIDSFLIWR LTGGRVHASD
     ATNAARTLMF DIHQGEWSKD ICELLDVPMS MLPEVRDCAA DFGTTDLFGG QVPILGVAGD
     QQAATIGQAC FQPGMMKSTY GTGCFALLNT GTQPVASQNR LLTTIAYQLD GQRTYALEGS
     IFIAGAAVQW LRDGLGIIEN AAQSGALAAR ADPAQNVILV PAFTGLGAPY WKPDCRGAMF
     GLTRNSGPAE FCKAALESVA YQTRDLWEAM QGDWGADADV ILRVDGGMSA SDWAMQGLAD
     RLGAPVDRPV MQETTALGAA WLAGMRAGVY PDQAGFAATW ALDARFTPKM VEGDREAAYR
     RWKAAVAAAM MV
//

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